ID   MTLD_MAGOY              Reviewed;         400 AA.
AC   L7IBL2; G4MS33; Q5EMU8;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Mannitol-1-phosphate 5-dehydrogenase;
DE            Short=M1PDH;
DE            Short=MPD;
DE            Short=MPDH;
DE            EC=1.1.1.17;
GN   ORFNames=OOU_Y34scaffold00406g8;
OS   Magnaporthe oryzae (strain Y34) (Rice blast fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=1143189;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Y34;
RA   Dong H.-T., Peng Y.-L., Chen B.-S., Li Y.-Z., Li D.-B.;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y34;
RX   PubMed=22876203; DOI=10.1371/journal.pgen.1002869;
RA   Xue M., Yang J., Li Z., Hu S., Yao N., Dean R.A., Zhao W., Shen M.,
RA   Zhang H., Li C., Liu L., Cao L., Xu X., Xing Y., Hsiang T., Zhang Z.,
RA   Xu J.-R., Peng Y.-L.;
RT   "Comparative analysis of the genomes of two field isolates of the rice
RT   blast fungus Magnaporthe oryzae.";
RL   PLoS Genet. 8:E1002869-E1002869(2012).
CC   -!- FUNCTION: Catalyzes the NAD(H)-dependent interconversion of D-fructose
CC       6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic
CC       pathway. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC         + H(+) + NADH; Xref=Rhea:RHEA:19661, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57634, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:61381; EC=1.1.1.17;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY849685; AAX07705.1; -; mRNA.
DR   EMBL; JH793115; ELQ40653.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7IBL2; -.
DR   SMR; L7IBL2; -.
DR   Proteomes; UP000011086; Unassembled WGS sequence.
DR   GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019594; P:mannitol metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   HAMAP; MF_00196; Mannitol_dehydrog; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR023028; Mannitol_1_phos_5_DH.
DR   InterPro; IPR000669; Mannitol_DH.
DR   InterPro; IPR013118; Mannitol_DH_C.
DR   InterPro; IPR013131; Mannitol_DH_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01232; Mannitol_dh; 1.
DR   Pfam; PF08125; Mannitol_dh_C; 1.
DR   PRINTS; PR00084; MTLDHDRGNASE.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..400
FT                   /note="Mannitol-1-phosphate 5-dehydrogenase"
FT                   /id="PRO_0000423547"
FT   ACT_SITE        221
FT                   /evidence="ECO:0000250"
FT   BINDING         12..23
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   400 AA;  44518 MW;  AAB005CB5590EADE CRC64;
     MSQTNGTHTK KAVHFGAGNI GRGFVACFLH NSGYEVVFAD VTDRTCDALN NQTSYKVIEV
     GAEGTEEKTI TNYRAINSKT KEDELLQEIA TADVVTCSVG PNILKFIAPV IAKGLDMRSE
     ELKPAAVIAC ENAIGATDTL AEHIKEHLPA TRVEDLSTRA RFANSAIDRI VPAQDPNSGL
     DVKLEKFYEW VVDRTPFADH EVPSIEGIHW VDNLEPYIER KLYTVNTGHA TAAYHGYNRQ
     KRTVYDALQD REIQSEVRRA LENTSKLITA KHGINPEEQQ AYVRKIMTRI GNPHLEDAVE
     RVGRAPLRKL SRKERFVGPA AELAEKGEDC SALLDAAEMA LRFQNVEEDA ESKELAKIMA
     ENSAEQVVSQ VCGLQPSEKL YPKMVEIVHR VQQDSMDDTE